TR201921815A2 - ENCAPSULATED ENZYMES AND THEIR USE IN TEXTILE APPLICATIONS - Google Patents
ENCAPSULATED ENZYMES AND THEIR USE IN TEXTILE APPLICATIONSInfo
- Publication number
- TR201921815A2 TR201921815A2 TR2019/21815A TR201921815A TR201921815A2 TR 201921815 A2 TR201921815 A2 TR 201921815A2 TR 2019/21815 A TR2019/21815 A TR 2019/21815A TR 201921815 A TR201921815 A TR 201921815A TR 201921815 A2 TR201921815 A2 TR 201921815A2
- Authority
- TR
- Turkey
- Prior art keywords
- enzyme
- concentration
- amylase
- solution
- alginate
- Prior art date
Links
- 102000004190 Enzymes Human genes 0.000 title claims abstract description 99
- 108090000790 Enzymes Proteins 0.000 title claims abstract description 99
- 239000004753 textile Substances 0.000 title claims abstract description 36
- 229940088598 enzyme Drugs 0.000 claims abstract description 98
- FHVDTGUDJYJELY-UHFFFAOYSA-N 6-{[2-carboxy-4,5-dihydroxy-6-(phosphanyloxy)oxan-3-yl]oxy}-4,5-dihydroxy-3-phosphanyloxane-2-carboxylic acid Chemical compound O1C(C(O)=O)C(P)C(O)C(O)C1OC1C(C(O)=O)OC(OP)C(O)C1O FHVDTGUDJYJELY-UHFFFAOYSA-N 0.000 claims abstract description 51
- 229940072056 alginate Drugs 0.000 claims abstract description 51
- 235000010443 alginic acid Nutrition 0.000 claims abstract description 51
- 229920000615 alginic acid Polymers 0.000 claims abstract description 51
- 102000013142 Amylases Human genes 0.000 claims abstract description 36
- 108010065511 Amylases Proteins 0.000 claims abstract description 36
- 239000004382 Amylase Substances 0.000 claims abstract description 31
- 102000016938 Catalase Human genes 0.000 claims abstract description 30
- 108010053835 Catalase Proteins 0.000 claims abstract description 30
- 108010059892 Cellulase Proteins 0.000 claims abstract description 30
- 235000019418 amylase Nutrition 0.000 claims abstract description 28
- 229940106157 cellulase Drugs 0.000 claims abstract description 23
- 238000000034 method Methods 0.000 claims description 39
- 239000011324 bead Substances 0.000 claims description 35
- IXPNQXFRVYWDDI-UHFFFAOYSA-N 1-methyl-2,4-dioxo-1,3-diazinane-5-carboximidamide Chemical compound CN1CC(C(N)=N)C(=O)NC1=O IXPNQXFRVYWDDI-UHFFFAOYSA-N 0.000 claims description 34
- 239000000661 sodium alginate Substances 0.000 claims description 34
- 235000010413 sodium alginate Nutrition 0.000 claims description 34
- 229940005550 sodium alginate Drugs 0.000 claims description 34
- 230000008569 process Effects 0.000 claims description 32
- 238000005538 encapsulation Methods 0.000 claims description 16
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 claims description 15
- 239000001110 calcium chloride Substances 0.000 claims description 10
- 229910001628 calcium chloride Inorganic materials 0.000 claims description 10
- 230000000743 anti-peroxide Effects 0.000 claims description 9
- 239000000648 calcium alginate Substances 0.000 claims description 9
- 235000010410 calcium alginate Nutrition 0.000 claims description 9
- 229960002681 calcium alginate Drugs 0.000 claims description 9
- OKHHGHGGPDJQHR-YMOPUZKJSA-L calcium;(2s,3s,4s,5s,6r)-6-[(2r,3s,4r,5s,6r)-2-carboxy-6-[(2r,3s,4r,5s,6r)-2-carboxylato-4,5,6-trihydroxyoxan-3-yl]oxy-4,5-dihydroxyoxan-3-yl]oxy-3,4,5-trihydroxyoxane-2-carboxylate Chemical compound [Ca+2].O[C@@H]1[C@H](O)[C@H](O)O[C@@H](C([O-])=O)[C@H]1O[C@H]1[C@@H](O)[C@@H](O)[C@H](O[C@H]2[C@H]([C@@H](O)[C@H](O)[C@H](O2)C([O-])=O)O)[C@H](C(O)=O)O1 OKHHGHGGPDJQHR-YMOPUZKJSA-L 0.000 claims description 9
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 claims description 2
- 229910052791 calcium Inorganic materials 0.000 claims description 2
- 239000011575 calcium Substances 0.000 claims description 2
- 210000003660 reticulum Anatomy 0.000 claims 1
- 229920001817 Agar Polymers 0.000 abstract description 15
- 239000008272 agar Substances 0.000 abstract description 13
- 229920000858 Cyclodextrin Polymers 0.000 abstract description 10
- HFHDHCJBZVLPGP-UHFFFAOYSA-N schardinger α-dextrin Chemical compound O1C(C(C2O)O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC(C(O)C2O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC2C(O)C(O)C1OC2CO HFHDHCJBZVLPGP-UHFFFAOYSA-N 0.000 abstract description 5
- 229920002521 macromolecule Polymers 0.000 abstract 1
- 239000000243 solution Substances 0.000 description 55
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 10
- 239000000499 gel Substances 0.000 description 10
- 238000012360 testing method Methods 0.000 description 10
- 239000004744 fabric Substances 0.000 description 8
- 230000000694 effects Effects 0.000 description 7
- 239000000203 mixture Substances 0.000 description 7
- 229920000936 Agarose Polymers 0.000 description 6
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 6
- 239000007864 aqueous solution Substances 0.000 description 5
- 238000004132 cross linking Methods 0.000 description 5
- 229940097362 cyclodextrins Drugs 0.000 description 5
- 229920000742 Cotton Polymers 0.000 description 4
- 230000004888 barrier function Effects 0.000 description 4
- 230000015572 biosynthetic process Effects 0.000 description 4
- 238000009990 desizing Methods 0.000 description 4
- 150000002978 peroxides Chemical class 0.000 description 4
- 239000000126 substance Substances 0.000 description 4
- 229920001353 Dextrin Polymers 0.000 description 3
- 239000004375 Dextrin Substances 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 229920002472 Starch Polymers 0.000 description 3
- 230000000593 degrading effect Effects 0.000 description 3
- 235000019425 dextrin Nutrition 0.000 description 3
- 238000004043 dyeing Methods 0.000 description 3
- 238000002474 experimental method Methods 0.000 description 3
- 238000009472 formulation Methods 0.000 description 3
- 150000004676 glycans Chemical class 0.000 description 3
- 229920001282 polysaccharide Polymers 0.000 description 3
- 239000005017 polysaccharide Substances 0.000 description 3
- 235000019698 starch Nutrition 0.000 description 3
- 239000008107 starch Substances 0.000 description 3
- 229920000297 Rayon Polymers 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 239000002775 capsule Substances 0.000 description 2
- 150000001875 compounds Chemical class 0.000 description 2
- 238000001816 cooling Methods 0.000 description 2
- 238000007730 finishing process Methods 0.000 description 2
- 239000000017 hydrogel Substances 0.000 description 2
- 229910052739 hydrogen Inorganic materials 0.000 description 2
- 239000001257 hydrogen Substances 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 239000011159 matrix material Substances 0.000 description 2
- 239000000155 melt Substances 0.000 description 2
- 239000011148 porous material Substances 0.000 description 2
- 230000006641 stabilisation Effects 0.000 description 2
- 238000011105 stabilization Methods 0.000 description 2
- AEMOLEFTQBMNLQ-AZLKCVHYSA-N (2r,3s,4s,5s,6r)-3,4,5,6-tetrahydroxyoxane-2-carboxylic acid Chemical compound O[C@@H]1O[C@@H](C(O)=O)[C@@H](O)[C@H](O)[C@@H]1O AEMOLEFTQBMNLQ-AZLKCVHYSA-N 0.000 description 1
- FBPFZTCFMRRESA-FSIIMWSLSA-N D-Glucitol Natural products OC[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-FSIIMWSLSA-N 0.000 description 1
- FBPFZTCFMRRESA-JGWLITMVSA-N D-glucitol Chemical compound OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-JGWLITMVSA-N 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 108010029541 Laccase Proteins 0.000 description 1
- 102000004882 Lipase Human genes 0.000 description 1
- 239000004367 Lipase Substances 0.000 description 1
- 108090001060 Lipase Proteins 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 102000003992 Peroxidases Human genes 0.000 description 1
- 241000199919 Phaeophyceae Species 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 239000000853 adhesive Substances 0.000 description 1
- 239000003905 agrochemical Substances 0.000 description 1
- 125000003275 alpha amino acid group Chemical group 0.000 description 1
- WQZGKKKJIJFFOK-PHYPRBDBSA-N alpha-D-galactose Chemical group OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@H]1O WQZGKKKJIJFFOK-PHYPRBDBSA-N 0.000 description 1
- 239000012736 aqueous medium Substances 0.000 description 1
- 239000002551 biofuel Substances 0.000 description 1
- 238000004061 bleaching Methods 0.000 description 1
- 239000007844 bleaching agent Substances 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 230000002925 chemical effect Effects 0.000 description 1
- 239000000084 colloidal system Substances 0.000 description 1
- 239000002131 composite material Substances 0.000 description 1
- 239000002537 cosmetic Substances 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 230000009088 enzymatic function Effects 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 238000007710 freezing Methods 0.000 description 1
- 230000008014 freezing Effects 0.000 description 1
- 125000002791 glucosyl group Chemical group C1([C@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 235000019421 lipase Nutrition 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 238000002844 melting Methods 0.000 description 1
- 230000008018 melting Effects 0.000 description 1
- 229910021645 metal ion Inorganic materials 0.000 description 1
- ZJQHPWUVQPJPQT-UHFFFAOYSA-N muscimol Chemical compound NCC1=CC(=O)NO1 ZJQHPWUVQPJPQT-UHFFFAOYSA-N 0.000 description 1
- 230000006855 networking Effects 0.000 description 1
- 239000007800 oxidant agent Substances 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 230000000704 physical effect Effects 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 239000000600 sorbitol Substances 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 230000036962 time dependent Effects 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 239000000080 wetting agent Substances 0.000 description 1
Classifications
-
- D—TEXTILES; PAPER
- D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
- D06M—TREATMENT, NOT PROVIDED FOR ELSEWHERE IN CLASS D06, OF FIBRES, THREADS, YARNS, FABRICS, FEATHERS OR FIBROUS GOODS MADE FROM SUCH MATERIALS
- D06M16/00—Biochemical treatment of fibres, threads, yarns, fabrics, or fibrous goods made from such materials, e.g. enzymatic
- D06M16/003—Biochemical treatment of fibres, threads, yarns, fabrics, or fibrous goods made from such materials, e.g. enzymatic with enzymes or microorganisms
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01J—CHEMICAL OR PHYSICAL PROCESSES, e.g. CATALYSIS OR COLLOID CHEMISTRY; THEIR RELEVANT APPARATUS
- B01J13/00—Colloid chemistry, e.g. the production of colloidal materials or their solutions, not otherwise provided for; Making microcapsules or microballoons
- B01J13/02—Making microcapsules or microballoons
- B01J13/04—Making microcapsules or microballoons by physical processes, e.g. drying, spraying
- B01J13/046—Making microcapsules or microballoons by physical processes, e.g. drying, spraying combined with gelification or coagulation
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01J—CHEMICAL OR PHYSICAL PROCESSES, e.g. CATALYSIS OR COLLOID CHEMISTRY; THEIR RELEVANT APPARATUS
- B01J13/00—Colloid chemistry, e.g. the production of colloidal materials or their solutions, not otherwise provided for; Making microcapsules or microballoons
- B01J13/02—Making microcapsules or microballoons
- B01J13/06—Making microcapsules or microballoons by phase separation
- B01J13/14—Polymerisation; cross-linking
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N11/00—Carrier-bound or immobilised enzymes; Carrier-bound or immobilised microbial cells; Preparation thereof
- C12N11/02—Enzymes or microbial cells immobilised on or in an organic carrier
- C12N11/04—Enzymes or microbial cells immobilised on or in an organic carrier entrapped within the carrier, e.g. gel or hollow fibres
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0065—Oxidoreductases (1.) acting on hydrogen peroxide as acceptor (1.11)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2405—Glucanases
- C12N9/2408—Glucanases acting on alpha -1,4-glucosidic bonds
- C12N9/2411—Amylases
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2405—Glucanases
- C12N9/2434—Glucanases acting on beta-1,4-glucosidic bonds
- C12N9/2437—Cellulases (3.2.1.4; 3.2.1.74; 3.2.1.91; 3.2.1.150)
-
- D—TEXTILES; PAPER
- D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
- D06L—DRY-CLEANING, WASHING OR BLEACHING FIBRES, FILAMENTS, THREADS, YARNS, FABRICS, FEATHERS OR MADE-UP FIBROUS GOODS; BLEACHING LEATHER OR FURS
- D06L1/00—Dry-cleaning or washing fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods
- D06L1/12—Dry-cleaning or washing fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods using aqueous solvents
- D06L1/14—De-sizing
-
- D—TEXTILES; PAPER
- D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
- D06M—TREATMENT, NOT PROVIDED FOR ELSEWHERE IN CLASS D06, OF FIBRES, THREADS, YARNS, FABRICS, FEATHERS OR FIBROUS GOODS MADE FROM SUCH MATERIALS
- D06M23/00—Treatment of fibres, threads, yarns, fabrics or fibrous goods made from such materials, characterised by the process
- D06M23/12—Processes in which the treating agent is incorporated in microcapsules
-
- D—TEXTILES; PAPER
- D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
- D06M—TREATMENT, NOT PROVIDED FOR ELSEWHERE IN CLASS D06, OF FIBRES, THREADS, YARNS, FABRICS, FEATHERS OR FIBROUS GOODS MADE FROM SUCH MATERIALS
- D06M15/00—Treating fibres, threads, yarns, fabrics, or fibrous goods made from such materials, with macromolecular compounds; Such treatment combined with mechanical treatment
- D06M15/01—Treating fibres, threads, yarns, fabrics, or fibrous goods made from such materials, with macromolecular compounds; Such treatment combined with mechanical treatment with natural macromolecular compounds or derivatives thereof
- D06M15/03—Polysaccharides or derivatives thereof
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Health & Medical Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Genetics & Genomics (AREA)
- Biochemistry (AREA)
- Microbiology (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Textile Engineering (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Dispersion Chemistry (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Or Physical Treatment Of Fibers (AREA)
- Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
- Enzymes And Modification Thereof (AREA)
Abstract
Mevcut buluş enzimlerin performansını arttırmak üzere makromoleküller ile enkapsüle edilerek tekstil uygulamalarında kullanılmaları ile ilgilidir. Buluş ile aljinat, agar ya da siklodekstrin arasından seçilen bir molekül ile enkapsüle edilen amilaz, selülaz ve katalaz arasından seçilen bir enzimin tekstil alanındaki kullanımları açıklanmaktadır.The present invention relates to the use of enzymes in textile applications by encapsulating them with macromolecules to improve their performance. The invention describes the textile uses of an enzyme selected from amylase, cellulase and catalase encapsulated with a molecule selected from alginate, agar or cyclodextrin.
Description
TARIFNAME ENKAPSÜLE EDILMIS ENZIMLER VE BUNLARIN TEKSTIL UYGULAMALARINDA KULLANIMI TEKNIK ALAN Bulus, enkapsüle edilmis enzimler ve bunlarin tekstil uygulamalarinda kullanimi ile Bulus özellikle, aljinat, agar ve siklodekstrin tarafindan enkapsüle edilmis amilaz, katalaz ve selülaz enzimleri ve bunlarin tekstil uygulamalarinda kullanimi ile ilgilidir. DESCRIPTION ENCAPSULATED ENZYMES AND THEIR TEXTILES USE IN APPLICATIONS TECHNICAL FIELD The invention relates to encapsulated enzymes and their use in textile applications. In particular, the invention provides amylase, catalase enzymes encapsulated by alginate, agar and cyclodextrin. and cellulase enzymes and their use in textile applications.
TEKNIGIN BILINEN DURUMU Enzimlerim tekstilden gidaya, ilaçtan kozmetik, deterjan, biyoyakita, endüstri ve biyoteknoloji alanlarinda çesitli uygulamalari bulunmaktadir. Enzimler protein yapida moleküllerdir ve dogada biyolojik ortamlarda çalismak üzere tasarlanmislardir. Aminoasit zincirleri enzimlerin üç boyutlu seklini, konformasyonunu ve fonksiyonunu belirlemektedir. Endüstriyel uygulamalarda maruz kaldiklari yüksek sicaklik, okside edici ajanlar, yüksek asidite ve alkalilik enzimlerin bu üç boyutlu yapisinin bozularak denatüre olmasina ve aktivitelerinin azalmasina sebep olmaktadir. Bu durum da enzimlerin verimli sekilde ve uzun süreli kullanilmasina engel olmaktadir. Bu nedenle enzimlerin stabilitesinin saglanarak enzim aktivitesinin devam ettirilmesi enzim uygulamalarinda en önemli hususlardan birisi olmaktadir. KNOWN STATE OF THE TECHNIQUE My enzymes are used in textiles, food, pharmaceuticals, cosmetics, detergents, biofuels, industry and It has various applications in biotechnology fields. Enzymes have a protein structure They are molecules and are designed to work in biological environments in nature. Amino acid chains determine the three-dimensional shape, conformation and function of enzymes. determines. The high temperatures they are exposed to in industrial applications cause oxidizing agents, high acidity and alkalinity denaturate enzymes by disrupting their three-dimensional structure. It causes the body to become swollen and its activities to decrease. In this case, enzymes are efficiently It prevents it from being used improperly and for a long time. Therefore, enzymes Maintaining enzyme activity by ensuring its stability is the most important method in enzyme applications. is one of the important issues.
Tekstil alaninda en çok kullanilan enzimler arasinda amilaz, selülaz, katalaz, proteaz, peroksidaz, lipaz ve lakkaz bulunmaktadir. Bu enziinler içerisinde ticari olarak en çok üretilen amilaz, katalaz ve selülaz enzimleridir. The most commonly used enzymes in the textile field include amylase, cellulase, catalase, protease, There are peroxidase, lipase and laccase. Among these enzymes, it is the most commercially available The enzymes produced are amylase, catalase and cellulase.
Amilaz enzimi hasil sökme enzimi olarak kullanilmakta olup pamuklu ürünlerdeki nisasta ve türevi hasil maddelerin suda çözünen dekstrin formuna parçalanarak hasilin uzaklastirilmasini saglamaktadir. Amylase enzyme is used as a degrading enzyme and is used to remove starch in cotton products. and its derivatives are broken down into water-soluble dextrin form and It ensures removal.
Katalaz enzimi ortamda bulunan hidrojen peroksitin parçalanmasini saglayarak boyama isleminden önce zararli olabilecek hidrojen peroksit kalintilarini uzaklastirmaktadir. Catalase enzyme breaks down the hydrogen peroxide in the environment, thus causing dyeing. It removes potentially harmful hydrogen peroxide residues before the process.
Selülaz enzimi pamuk, viskon, keten vb. gibi selülozik kumas ve karisimlarinin tüylerini gidererek bitim islemlerinde tuseyi olumlu yönde etkilemek amaciyla kullanilmaktadir. Cellulase enzyme is used in cotton, viscose, linen etc. fluff of cellulosic fabrics and blends such as It is used to positively affect the touch in finishing processes.
Konvensiyonel tekstil ürünlerinde bu enzimler bir solüsyon içerisinde hazirlanip kullanim amacina göre çektirme, kasar ve fular yöntemleriyle kumasa uygulanmaktadir. Bu uygulamalar, 30 ile 95 0C arasi sicakliklarda ve farkli pH degerlerinde yapilmaktadir. In conventional textile products, these enzymes are prepared and used in a solution. It is applied to the fabric by shrinking, bleaching and foulard methods depending on its purpose. This Applications are made at temperatures between 30 and 95 0C and at different pH values.
Uygulamalarin çikabildigi yüksek sicaklilar enzimlerin yapisinin bozularak denatüre olmasina ve aktivitelerinin kaybolmasina sebep olmaktadir. The high temperatures that applications can cause deteriorate the structure of enzymes and cause them to denature. causes it to become damaged and its activities to disappear.
Enzimler mevcut ticari ürünlerde sulu ortamda hazirlanan sorbitol, gliserol, seker, tuz ve çesitli islatici ajanlar içeren formülasyonlar seklinde üretilmektedir. Bu ürünlerde enzim yeteri kadar stabil kalamamakta, depolama ve tekstil uygulamalari sirasinda aktiviteleri düsmektedir. Bu sebepten dolayi enzim içeren tekstil ürünlerinin raf` ömürleri 3 ile 6 ay arasinda degisip maksimum 1 yil olabilinektedir. Enzymes are present in commercial products prepared in aqueous media such as sorbitol, glycerol, sugar, salt and It is produced in the form of formulations containing various wetting agents. Enzyme in these products It does not remain stable enough and its activities during storage and textile applications is falling. For this reason, the shelf life of textile products containing enzymes is 3 to 6 months. It may vary between 1 year and 1 year maximum.
Teknigin bilinen durumunda enzimlerin stabilitesini ve raf ömrünü uzatmaya yönelik olarak uygulanan çesitli yöntemler bulunmaktadir. Bunlardan birisi enzimin büyük bir molekül tarafindan enkapsüle edilmis sekilde bulundugu kompozit malzemelerin olusturulmasidir. In the state of the art, it is aimed to extend the stability and shelf life of enzymes. There are various methods applied. One of these is that the enzyme has a large Composite materials are encapsulated by molecules is the creation.
EP2698434A1 sayili patent basvurusunda enzimlerin enkapsülasyon yoluyla korunabildigi aç iklanmaktadir. In the patent application numbered EP2698434A1, it is stated that enzymes can be protected by encapsulation. is getting hungry.
Kumar R, Entrapment of a-amylase in alginate beads: Single step protocol for purification and thermal stabilization makalesinde a-amilazin aljinat tarafindan hapsedilerek termal stabilitesinin arttirildigi açiklanmaktadir. Kumar R, Entrapment of a-amylase in alginate beads: Single step protocol for purification In the and thermal stabilization article, a-amylazine is trapped by alginate and thermally stabilized. It is explained that its stability is increased.
Tekstil uygulamalarinda ihtiyaç duyulan kosullarin saglanmasi için belirli enzimlerin aktivitesi ve dolayisiyla performansi korunarak stabilize edilmesine ihtiyaç devam etmektedir. Ayrica raf ömrü, serbest haldeki enzime kiyasla daha uzun olan ürünler elde edilmesi de tekstil uygulamalarinda çözülmesi amaçlanan problemler arasinda yer almaktadir. Certain enzymes are used to provide the conditions needed in textile applications. There continues to be a need for stabilization by preserving its activity and therefore its performance. It does. In addition, products with a longer shelf life are obtained compared to the free enzyme. is among the problems aimed to be solved in textile applications. is taking.
Sonuç olarak mevcut çözümlerin konu hakkindaki yetersizligi nedeniyle ilgili teknik alanda bir gelistirme yapilmasi gerekli kilinmistir. As a result, due to the inadequacy of existing solutions on the subject, the relevant technical It was deemed necessary to make development in this field.
BULUSUN KISA AÇIKLAMASI Mevcut bulus, yukarida bahsedilen gereksinimleri karsilayan ve ilave bazi avantajlar getiren, amilaz, selülaz ve katalaz arasindan seçilen bir enzimin aljinat, agar ve siklodekstrinden biri ile enkapsüle edilmesi için prosesler ve bu proseslerden elde edilen enkapsüle amilaz, enkapsüle selülaz ve enkapsüle katalazin tekstil uygulamalarinda kullanimlari ile ilgilidir. BRIEF DESCRIPTION OF THE INVENTION The present invention meets the above-mentioned requirements and provides some additional advantages. alginate, agar and processes for encapsulating with one of the cyclodextrins and the results obtained from these processes encapsulated amylase, encapsulated cellulase and encapsulated catalazine in textile applications related to their use.
Bulusun Öncelikli amaci, tekstil uygulamalarinda kullanilmak üzere enzim performansinin arttirilmasini saglayan prosesler temin etmektir. The primary purpose of the invention is to improve enzyme performance for use in textile applications. is to provide processes that enable it to be increased.
Bulusun öncelikli amaci, tekstil uygulamalarinda kullanilmak üzere enzim aktivitesinin arttirilmasini saglayan prosesler temin etmektir. The primary purpose of the invention is to improve enzyme activity for use in textile applications. is to provide processes that enable it to be increased.
Bulusun bir diger amaci, tekstil uygulamalarinda kullanilmak üzere enzim dayanikliliginin ve raf ömrünün arttirilmasini saglayan prosesler temin etmektir. Another purpose of the invention is to improve enzyme stability for use in textile applications. and to provide processes that increase shelf life.
Yukarida bahsedilen ve asagidaki detayli anlatimdan ortaya çikacak tüm amaçlari gerçeklestirmek üzere mevcut bulus, amilaz, selülaz ve katalaz arasindan seçilen bir enzimin aljinat ile enkapsülasyon yoluyla aljinat boncuklarinin üretilmesi için bir proses temin etmektedir. All purposes mentioned above and which will emerge from the detailed explanation below. The present invention uses a compound selected from amylase, cellulase and catalase to carry out A process for producing alginate beads by encapsulation of enzyme with alginate provides.
Bulusun tercih edilen bir yapilanmasmda, bahsedilen proses sulu sodyum aljinat çözeltisine bahsedilen enzimlerden en az birinin eklenmesi adimini içermektedir. In a preferred embodiment of the invention, the said process is carried out using aqueous sodium alginate. It includes the step of adding at least one of the enzymes mentioned to the solution.
Bulusun tercih edilen bir yapilanmasinda, bahsedilen sodyum aljinat çözeltisinin konsantrasyonu agirlikça %0,25-2,00 araligindadir. In a preferred embodiment of the invention, said sodium alginate solution is Its concentration is between 0.25-2.00% by weight.
Bulusun tercih edilen bir yapilanmasinda, bahsedilen sodyum aljinat çözeltisinin konsantrasyonu agirlikça %1 ,0°dir. In a preferred embodiment of the invention, said sodium alginate solution is Its concentration is 1.0% by weight.
Bulusun tercih edilen bir yapilanmasinda, bahsedilen proses enzim içeren sulu sodyum aljinat çözeltisinin kalsiyum klorür içeren bir çözeltiye damlatilarak kalsiyum aljinat boncuklarinin elde edilmesi adimini içermektedir. In a preferred embodiment of the invention, said process involves enzyme-containing aqueous sodium chloride. calcium alginate by dropping the alginate solution into a solution containing calcium chloride. It includes the step of obtaining the beads.
Bulusun tercih edilen bir yapilanmasinda, bahsedilen kalsiyum klorür çözeltisindeki kalsiyum klorürün inolaritesi (LI-1,0 M araligindadir. In a preferred embodiment of the invention, in said calcium chloride solution The inolarity of calcium chloride is in the range (LI-1.0 M).
Bulusun tercih edilen bir diger yapilanmasmda, bahsedilen kalsiyum klorür çözeltisindeki kalsiyum klorürün molaritesi 0,2 M”dir. In another preferred embodiment of the invention, the calcium chloride solution in question The molarity of calcium chloride is 0.2 M.
Bulusun tercih edilen bir baska yapilanmasinda, bahsedilen enzim amilazdir. In another preferred embodiment of the invention, said enzyme is amylase.
Bulusun tercih edilen bir baska yapilanmasinda, amilazin sodyum aljinat çözeltisindeki konsantrasyonu agirlikça %3-207dir. In another preferred embodiment of the invention, amylazine in sodium alginate solution Its concentration is 3-207% by weight.
Bulusun tercih edilen bir diger yapilanmasinda, amilazin sodyum aljinat çözeltisindeki konsantrasyonu agirlikça %5-8°dir. In another preferred embodiment of the invention, amylazine in sodium alginate solution Its concentration is 5-8% by weight.
Bulusun tercih edilen bir yapilanmasmda, bahsedilen enzim katalazdir. In a preferred embodiment of the invention, said enzyme is catalase.
Bulusun tercih edilen bir diger yapilanmasinda, katalazin sodyum aljinat çözeltisindeki konsantrasyonu agirlikça %1 -5 ”tir. In another preferred embodiment of the invention, catalazine in sodium alginate solution Its concentration is 1-5% by weight.
Bulusun tercih edilen bir diger yapilanmasinda, katalazin sodyum aljinat çözeltisindeki konsantrasyonu agirlikça %1 -2°dir. In another preferred embodiment of the invention, catalazine in sodium alginate solution Its concentration is 1-2% by weight.
Bulusun tercih edilen bir yapilanmasinda, bahsedilen enzim selülazdir. In a preferred embodiment of the invention, said enzyme is cellulase.
Bulusun tercih edilen bir diger yapilanmasinda, selülazin sodyum aljinat çözeltisindeki konsantrasyonu agirlikça %5-20”dir Bulusun tercih edilen bir diger yapilanmasinda, selülazin sodyum aljinat çözeltisindeki konsantrasyonu agirlikça % 10- l 5 ”tir. In another preferred embodiment of the invention, cellulazine is dissolved in sodium alginate solution. concentration is 5-20% by weight In another preferred embodiment of the invention, cellulazine is dissolved in sodium alginate solution. Its concentration is 10-15% by weight.
Yukarida bahsedilen ve asagidaki detayli anlatimdan ortaya çikacak tüm amaçlari gerçeklestirmek üzere mevcut bulus, aljinat ile enkapsüle bir enzimin tekstil uygulamalarinda kullanimini temin etmekte olup, bahsedilen enzim ci-amilaza selülaz ve katalaz arasindan seçilmektedir. All purposes mentioned above and which will emerge from the detailed explanation below. In order to realize the present invention, an enzyme encapsulated with alginate is used in textile It ensures its use in applications, and the said enzyme is ci-amylase cellulase and It is selected from catalase.
Bulusun tercih edilen bir yapilanmasinda, bahsedilen enzim amilazdir ve bahsedilen tekstil uygulamasi hasil sökme uygulamasidir. In a preferred embodiment of the invention, said enzyme is amylase and said textile The application is a disassembly application.
Bulusun tercih edilen bir diger yapilanmasinda, bahsedilen enzim katalazdir ve bahsedilen tekstil uygulamasi antiperoksit enzim uygulamasidir. In another preferred embodiment of the invention, said enzyme is catalase and said Textile application is antiperoxide enzyme application.
Bulusun tercih edilen bir diger yapilanmasinda, bahsedilen enzim selülazdir ve bahsedilen tekstil uygulamasi anti-pilling uygulamasidir. In another preferred embodiment of the invention, said enzyme is cellulase and said The textile application is an anti-pilling application.
Bulusun yapisal ve karakteristik özellikleri ve tüm avantajlari asagida verilen detayli açiklama sayesinde daha net olarak anlasilacaktir ve bu nedenle degerlendirmenin de bu detayli açiklama göz önüne alinarak yapilmasi gerekmektedir. The structural and characteristic features and all the advantages of the invention are detailed below. Thanks to the explanation, it will be understood more clearly and therefore the evaluation will also be It should be done taking into account the detailed explanation.
BULUSUN DETAYLI AÇIKLAMASI Amilaz enzimi hasil sökme enzimi olarak kullanilmakta olup painuklu ürünlerdeki nisasta ve türevi hasil maddelerini suda çözünen dekstrin formuna parçalanarak hasilin uzaklastirilmasini saglamaktadir. DETAILED DESCRIPTION OF THE INVENTION Amylase enzyme is used as a degrading enzyme and it is used to remove starch in raw products. and its derivatives are decomposed into water-soluble dextrin form and It ensures removal.
Katalaz enzimi ortamda bulunan hidrojen peroksitin parçalanmasini saglayarak boyama isleminden önce zararli olabilecek hidrojen peroksit kalintilarini uzaklastirmaktadir. Catalase enzyme breaks down the hydrogen peroxide in the environment, thus causing dyeing. It removes potentially harmful hydrogen peroxide residues before the process.
Selülaz enzimi ise pamuk, viskon, keten vb. gibi selülozik kumas ve karisimlarinin tüylerini gidererek bitim islemlerinde tuseyi olumlu yönde etkilemek amaciyla kullanilmaktadir. Cellulase enzyme is used in cotton, viscose, linen, etc. cellulosic fabrics and blends such as In order to positively affect the touch in finishing processes by removing its hair. is used.
Mevcut bulus ile amilaz, katalaz ve selülaz enzimlerinin yukarida bahsedilen tekstil uygulamalarindaki performanslarinin, konvansiyonel solüsyon sistemlerine kiyasla enkapsüle edildiklerinde daha yüksek oldugu bulunmustur. Bulus sayesinde daha az konsantrasyonda enzim kullanilarak daha etkin sonuçlar elde edilebilmekte, enzimin daha yüksek sicakliklarda daha fazla dayanikli olmasi saglanmaktadir. Ayrica enkapsülasyon yoluyla hazirlanan enzim sistemlerinin raf ömrünün serbest halde enzim içeren ürünlerden daha uzun oldugu tespit edilmistir. With the present invention, amylase, catalase and cellulase enzymes are used in the above-mentioned textile their performance in applications compared to conventional solution systems. It was found to be higher when they were encapsulated. Thanks to the invention, less More effective results can be obtained by using enzyme at higher concentration, It is ensured to be more durable at high temperatures. Also encapsulation The shelf life of enzyme systems prepared by It was found to be longer.
Soguk su bölgelerinde yetisen kahverengi yosundan elde edilen aljinat lineer bir polisakkarit olup ß-D-manuronik asit (M) ve a-L-guluronik asitin (G) 1-4 baglarindan meydana gelmektedir. Bilesiini ve zincir boyunca dizilimi çesitlilik göstermektedir. (Zhang and Zhao 2007; Lertsutthiwong et al. 2008). Söz konusu polisakkarit, metal iyonlari kullanilarak jellestirildikten sonra agrokimyasallarin sürekli salimi amaciyla Aljinatm kimyasal yapisi Formül 1 ile gösterilmektedir. Alginate obtained from brown algae growing in cold water regions is a linear It is a polysaccharide and consists of 1-4 bonds of ß-D-manuronic acid (M) and α-L-guluronic acid (G). is occurring. Its composition and arrangement along the chain vary. (zhang and Zhao 2007; Lertsutthiwong et al. 2008). The polysaccharide in question contains metal ions for the continuous release of agrochemicals after gelling using The chemical structure of alginate is shown in Formula 1.
Formül 1 Siklodekstrinler Ot-(l,4) baglari ile birlesen glikoz birimlerinden (d-D-glükopiranoz) meydana gelen kompleks polisakkaritlerdir. Hidroksil gruplarinin disa dönük yerlesimi ve konik yapisi nedeniyle kendine özgü fizikokimyasal özellikleri bulunan Siklodekstrinler içerisinde bulunun boslukta hidrofobik bilesikleri tasiyabilmekte ayni zamanda sulu ortamda çözünebilmektedir (Britto et al. 2004). Siklodekstrinler çok sayida molekül ile inklüzyon kompleksi olusturma kapasitesi nedeniyle yaygin olarak kullanilmaktadir (PérezMartinez et al. 1999; De Carvalho and de Alves Pinto 2012; Morin-Crini and Crini kimyasal yapisi Formül 2 ile gösterilmektedir. Formula 1 Cyclodextrins are composed of glucose units (d-D-glucopyranose) joined by Ot-(1,4) bonds. They are complex polysaccharides that occur. Outward orientation of hydroxyl groups and Cyclodextrins have unique physicochemical properties due to their conical structure. It can carry hydrophobic compounds in the space inside it and also aqueous It can dissolve in the environment (Britto et al. 2004). Cyclodextrins are composed of many molecules. It is widely used due to its ability to form inclusion complexes. (PérezMartinez et al. 1999; De Carvalho and de Alves Pinto 2012; Morin-Crini and Crini Its chemical structure is shown by Formula 2.
Agar, agaroz ve agaropektin karisimindan meydana gelen hidrofilik bir kolloiddir. Agarin içerisindeki agaroz agarin yaklasik %701ini meydana getirmektedir. Agaroz hücreleri enkapsüle etmek üzere bir matriks olarak kullanilabilmektedir. Agaroz, termal olarak çapraz baglanabilen, tekrar eden 1,3-linkli-d-galakt0z ve 1,4-linkli- 3,6-anhidr0-0t-l- galaktopiranoz birimlerini içermektedir. (Normand ve ark., 2000). Agaroz, genis çapli hücre içi hidrojen baglarinin olusup kalin yiginlar seklinde agrega olan çifte sarmal yapiyi meydana getirdigi için hücre enkapsülasyonu için kullanilabilmektedir (Xiong ve ark., 2005). Bahsedilen hidrojen baglari ile zamana bagli mekanik özelliklere sahip hidrojelleri meydana getirmektedir. Buna bagli olarak agar, sicak sulu bir çözeltinin sogutulmasiyla tersinir bir biçimde jel olusturabilmektedir. Agar jeli isitmayla erimekte sogutmayla tekrar eski haline geri dönmektedir. Agarin %l,5°lik çözeltisi için tipik jel sicakligi 35-45 C'dir ve bu nedenle çok düsük konsantrasyonlarda çok sert jeller olusturabilmektedir. Agarozun kimyasal yapisi Formül 3 ile gösterilmektedir. Agar is a hydrophilic colloid consisting of a mixture of agarose and agaropectin. agarine The agarose in it constitutes approximately 701% of the agar. agarose cells It can be used as a matrix for encapsulation. Agarose, thermally cross-linkable repeating 1,3-linked-d-galactoz and 1,4-linked-3,6-anhydr0-0t-1- Contains galactopyranose units. (Normand et al., 2000). Agarose, large diameter double helix structure where intracellular hydrogen bonds form and aggregate in the form of thick stacks It can be used for cell encapsulation because it produces 2005). Hydrogels with time-dependent mechanical properties with the mentioned hydrogen bonds It creates. Accordingly, agar is prepared by cooling a hot aqueous solution. It can form gel reversibly. Agar gel melts with heating and melts again with cooling. returns to its former state. Typical gel temperature for a 1.5% solution of agar is 35-45°C. and therefore can form very hard gels at very low concentrations. of agarose Its chemical structure is shown by Formula 3.
Agarmu > (11050; Agariipcctin Formül 3 Enzimler siklodekstrin, agar ve aljinat içinde hapsedilme yoluyla enkapsüle edilebilmektedir. Farkli konsantrasyonlarda hazirlanan siklodekstrin, agar ve aljinat çözeltilerine farkli konsantrasyonlarda eklenen enzimler farkli kimyasal ve fiziksel mekanizmalar ile bu moleküllerden elde edilen matris içerisinde hapsedilmektedir. Agarmu > (11050; Agariipcctin Formula 3 Enzymes are encapsulated by entrapment in cyclodextrin, agar and alginate. can be done. Cyclodextrin, agar and alginate prepared in different concentrations Enzymes added to solutions at different concentrations cause different chemical and physical effects. It is trapped in the matrix obtained from these molecules by mechanisms.
Mevcut bulus amilaz, selülaz ve katalaz arasindan seçilen bir enzimin aljinat, agar ve siklodesktrinden biri ile enkapsüle edilmesi için prosesler temin etmektedir. Aljinat ile enkapsülasyon iyonik çapraz baglama yoluyla yapilmaktadir. Agar ile enkapsülasyon fiziksel olarak (erime, set etme, dondurma) network olusturma yoluyla yapilmaktadir. The present invention involves the preparation of an enzyme selected from amylase, cellulase and catalase in alginate, agar and provides processes for encapsulating it with one of the cyclodextrins. with alginate Encapsulation is done through ionic cross-linking. Encapsulation with agar It is done physically (melting, setting, freezing) through networking.
Aljinat ve agar enkapsülasyonda sistem hidrojel yapiya sahiptir ve enzim gözeneklerden salim yoluyla yapilmaktadir. Siklodekstriii ile enkapsülasyon ise içerisine yükleme seklinde yapilabilmektedir. In alginate and agar encapsulation, the system has a hydrogel structure and the enzyme is absorbed through the pores. It is done through release. Encapsulation with cyclodextric It can be done as follows.
Mevcut bulus ayrica aljinat, agar ya da siklodekstrin ile enkapsüle edilen bir enzimin tekstil uygulamalarinda kullanimini temin etmekte olup, burada bahsedilen enzim U.- amilaz, selülaz ve katalaz arasindan seçilmektedir. Enzim amilaz oldugunda bahsedilen tekstil uygulamasi hasil sökme uygulamasi olabilir. Enzim selülaz oldugunda bahsedilen tekstil uygulamasi antipilling enzim uygulamasi olabilir. Enzim katalaz oldugunda bahsedilen tekstil uygulamasi antiperoksit olabilir. The present invention also includes the use of an enzyme encapsulated with alginate, agar or cyclodextrin. It ensures its use in textile applications, and the enzyme mentioned here is U.- is selected from amylase, cellulase and catalase. When the enzyme amylase is mentioned Textile application may be a disassembly application. When the enzyme cellulase is mentioned Textile application can be antipilling enzyme application. When the enzyme is catalase Said textile application may be antiperoxide.
Mevcut basvuruda “tekstil uygulamalari” ifadesi tekstil alaninda enzim kullanilarak gerçeklestirilen islemleri ifade etmektedir. In the current application, the term “textile applications” is used in the textile field using enzymes. represents the operations performed.
Mevcut basvuruda “hasil sökme uygulamasi” tekstil alaninda amilaz enzimi kullanilarak gerçeklestirilen, pamuklu ürünlerdeki nisasta ve türevi hasil maddelerin suda çözünen dekstrin formuna parçalanarak uzaklastirilmasini saglamak üzere yapilan islemleri ifade etmektedir. In the current application, “desizing application” is applied in the textile field using amylase enzyme. water-soluble degradation of starch and its derivatives in cotton products. It refers to the processes carried out to ensure that it is removed by breaking down into dextrin form. It does.
Mevcut basvuruda “antiperoksit enzim uygulamasi” tekstil alaninda katalaz enzimi kullanilarak gerçeklestirilen, boyaina isleininden önce kumas üretiminde zararli olabilecek hidrojen peroksit kalintilarini hidrojen peroksiti parçalayarak uzaklastirilmasini saglamak üzere yapilan islemleri ifade etmektedir. In the current application, “antiperoxide enzyme application” refers to catalase enzyme in the textile field. which may be harmful in fabric production before the dyeing process. ensuring that hydrogen peroxide residues are removed by breaking down the hydrogen peroxide It refers to the transactions carried out as follows.
Mevcut basvuruda “anti-pilling uygulamasi” tekstil alaninda selülaz enzimi kullanilarak gerçeklestirilen örme kumas üretiminde kaliteye etki eden önemli parametrelerden birisi olan boncuklanma yani pilling olusumunu azaltmak yani kumasa antipilling özellik kazandirmak üzere yapilan islemleri ifade etmektedir. In the current application, “anti-pilling application” is applied in the textile field using cellulase enzyme. One of the important parameters affecting the quality in knitted fabric production is To reduce pilling formation, that is, to provide antipilling properties to the fabric. It refers to the transactions made to gain profit.
Aliinat ile enkapsülasyon Mevcut bulus amilaz, selülaz ve katalaz arasindan seçilen bir enzimin aljinat ile enkapsülasyon yoluyla kalsiyum aljinat boncuklarinin üretilmesi için bir proses ve elde edilen alj inat boncuklarinin tekstil uygulamalarinda kullanimini temin etmektedir. Encapsulation with aliinate The present invention involves the synthesis of an enzyme selected among amylase, cellulase and catalase with alginate. A process for producing calcium alginate beads by encapsulation and the resulting It ensures the use of the obtained alginate beads in textile applications.
Bulus konusu proseste sodyum aljinat çözeltisine ainilaz, selülaz ya da katalaz enzimlerinden en az biri eklenerek enzim içeren sodyum aljinat çözeltisi hazirlanmakta; ve enzim içeren sodyum aljinat çözeltisi bir kalsiyum klorür çözeltisine damlatilarak söz konusu enzim ya da enziinleri içeren kalsiyum aljinat boncuklari elde edilmektedir. Bu sayede aljinat ile enkapsülasyon, sodyum aljinat çözeltisinin Ca2+ içeren ortamda iyonik çapraz baglanmasi ile saglanmaktadir. In the process of the invention, ainylase, cellulase or catalase is added to sodium alginate solution. Sodium alginate solution containing enzyme is prepared by adding at least one of the enzymes; And enzyme-containing sodium alginate solution was dropped into a calcium chloride solution. Calcium alginate beads containing the enzyme or enzymes in question are obtained. This Thus, encapsulation with alginate enables the sodium alginate solution to become ionic in the environment containing Ca2+. It is achieved by cross-linking.
Bulusun tercih edilen bir yapilanmasinda, bahsedilen enzim amilazdir. Amilaz konsantrasyonu arttikça sistemdeki amilaz/aljinat orani artmakta ve aljinat orani azalmaktadir, Bu da porlari daha genis olan daha yumusak jel boncuklar elde edilmesine neden olmaktadir. Dolayisiyla örnegin agirlikça %10 amilaz konsantrasyonuna sahip aljinat boncuklar, agirlikça %7 amilaz konsantrasyonuna sahip aljinat boncuklar kadar dayanikli degildir, daha zayif bir ainilaz bariyerine sahiptir ve dolayisiyla amilaz aktivitesini daha az koruyabilmektedir. Diger önemli bir etken ise belli konsantrasyonun üstünde amilaz enziininin aljinat jel yapisini kismen degrade etme yoluyla zayiflatabilmesidir. Mevcut bulus ile amilazin sulu sodyum aljinat çözeltisindeki konsantrasyonu agirlikça %3-20 oldugunda elde edilen aljinat boncuklarin hasil sökme uygulamasinda etkili oldugu ve amilazin sulu sodyum aljinat çözeltisindeki konsantrasyonu agirlikça %5-8 oldugunda elde edilen aljinat boncuklarin hasil sökme uygulamasinda en yüksek performansi gösterdigi bulunmustur. In a preferred embodiment of the invention, said enzyme is amylase. amylase As the concentration increases, the amylase/alginate ratio in the system increases and the alginate ratio increases. This results in softer gel beads with wider pores. causes. Therefore, for example, with an amylase concentration of 10% by weight alginate beads, as much as alginate beads with 7% amylase concentration by weight is not resistant, has a weaker ainylase barrier and therefore less able to maintain its activity. Another important factor is the concentration of a certain concentration. by partially degrading the alginate gel structure of amylase enzyme on It can weaken. With the present invention, amylazine in aqueous sodium alginate solution The disassembly of the alginate beads obtained when the concentration is 3-20% by weight It is effective in the application of amylazine in aqueous sodium alginate solution. The disassembly of the alginate beads obtained when the concentration is 5-8% by weight It has been found to show the highest performance in its application.
Bulusun tercih edilen bir diger yapilanmasinda bahsedilen enzim katalazdir. Mevcut bulus ile katalazin sulu sodyum aljinat çözeltisindeki konsantrasyonu agirlikça %1-5 oldugunda elde edilen aljinat boncuklarin peroksit enzim uygulamasinda en yüksek performansi gösterdigi bulunmustur. Bulusun tercih edilen bir yapilanmasinda katalazin sulu sodyum aljinat Çözeltisindeki konsantrasyonu agirlikça %1-2°dir. Bu oran ile elde edilen aljinat boncuklarda jel yapi etkilenmemektedir. Ayrica maliyet açisindan da bu oran tercih edilmektedir. In another preferred embodiment of the invention, the enzyme mentioned is catalase. current invention and when the concentration of catalazine in aqueous sodium alginate solution is 1-5% by weight The obtained alginate beads showed the highest performance in peroxide enzyme application. has been found to show. In a preferred embodiment of the invention, catalazine aqueous sodium Its concentration in alginate solution is 1-2% by weight. The alginate obtained with this ratio The gel structure of the beads is not affected. Additionally, this ratio is preferred in terms of cost. is done.
Bulusun tercih edilen bir diger yapilanmasinda bahsedilen enzim selülazdir. Mevcut bulus ile selülazin sulu sodyum alj inat çözeltisindeki konsantrasyonu agirlikça %5 -20 oldugunda elde edilen alj inat boncuklarin kumasta boncuklanma uygulamasinda en yüksek performansi gösterdigi bulunmustur. Bulusun tercih edilen bir yapilanmasinda selülazm sulu sodyum aljinat çözeltisindeki konsantrasyonu agirlikça %10-15°dir. Bu oran ile elde edilen aljinat boncuklarda jel yapi etkilenmemektedir. Ayrica maliyet açisindan da bu oran tercih edilmektedir. In another preferred embodiment of the invention, the enzyme mentioned is cellulase. current invention and when the concentration of cellulazine in aqueous sodium alginate solution is 5 - 20% by weight The obtained alginate beads have the highest rate in fabric pilling application. It has been found to show good performance. In a preferred embodiment of the invention, cellulase Its concentration in aqueous sodium alginate solution is 10-15% by weight. With this ratio you get The gel structure of the alginate beads obtained is not affected. In addition, in terms of cost, this rate is preferred.
Bulus konusu proseste kullanilan sodyum aljinat çözeltisinin ve kullanilan kalsiyum klorür çözeltisinin konsantrasyonlarini elde edilen aljinat boncuklarini önemli ölçüde etkilemektedir. Düzgün küresel yapida ve boyut dagiliminda bir birine yapismayan kapsüller elde etmek üzere bahsedilen sodyum aljinat çözeltisinin konsantrasyonu agirlikça çözeltisindeki kalsiyum klorürün molaritesi 0,1-1,0 M araliginda, tercihen 0,2 M°dir. Bu konsantrasyonlarda hem düzgün küresel sekilde ve esit büyüklükte kapsüller elde edilmis, hem de elde edilen optimum sertlikte jel yapiyla daha kontrollü enzim salimi ve performansi saglanmistir. Örnekler göre farkli konsantrasyonlarda enzim eklenerek enzim içeren aljinat çözeltileri çözeltilerine damlatilarak kalsiyum alj inat boncuklari elde edilmistir. Örnek 1 - Aliinat ile enkapsüle amilaz Hasil sökme uygulamasi için agirlikça %1,0”lik sodyum aljinat sulu çözeltilerine agirlikça Bu çözeltiler 0,2 Mllik kalsiyum klorür çözeltilerine dainlatilarak kalsiyum aljinat boncuklari elde edildi. Uygulamadaki performansini test etmek için amilaz enzimi içeren sodyum aljinat çözeltileri ve kalsiyum aljinat boncuk örnekleri 60 OC”de 30 dk hasil sökme uygulamasina maruz birakildi. Elde edilen sonuçlar Tablo l”de verilmistir. TEGEWA testi ile enzim performanslari ölçüldü. TEGEWA degeri enzim performansi ile dogru orantili olarak degismektedir. The sodium alginate solution and calcium chloride used in the process of the invention The concentrations of the solution significantly increased the obtained alginate beads. It affects. Non-adhesive with uniform spherical structure and size distribution concentration of said sodium alginate solution to obtain capsules The molarity of calcium chloride in solution is in the range of 0.1-1.0 M, preferably 0.2 M°. This capsules of uniform spherical shape and equal size were obtained at different concentrations. and more controlled enzyme release and performance has been achieved. Examples Alginate solutions containing enzymes were prepared by adding enzymes at different concentrations according to Calcium alginate beads were obtained by dropping them into the solutions. Example 1 - Amylase encapsulated with aliinate For stripping application, add 1.0% by weight sodium alginate aqueous solutions. These solutions were added to 0.2 ml calcium chloride solutions to form calcium alginate. beads were obtained. Containing amylase enzyme to test its performance in practice Sodium alginate solutions and calcium alginate bead samples were removed for 30 minutes at 60 °C. was subjected to the practice. The results obtained are given in Table 1. TEGEWA test Enzyme performances were measured with . TEGEWA value is directly proportional to enzyme performance It changes to .
Enkapsülasyon metodu Amilaz konsantrasyonu (0/0) TEGEWA A1 jinat boncuk 7 9 Aljinat boiicuk 10 8 Aljinat çözeltisi 7 8 Aljinat çözeltisi 10 8 Bu sonuçlara göre en iyi enzim performansi agirlikça %7' enzim konsantrasyonu olan aljinat boncuklarinda kaydedilmistir. Böylelikle daha az enzim içermesine ragmen agirlikça %7 enzim konsantrasyonu olan aljinat boncuklarinin hasil sökme uygulamasinda daha iyi sonuçlar elde edildigi bulunmustur. Encapsulation method Amylase concentration (0/0) TEGEWA A1 jinat beads 7 9 Alginate boiicuk 10 8 Alginate solution 7 8 Alginate solution 10 8 According to these results, the best enzyme performance was obtained with 7% enzyme concentration by weight. was recorded in alginate beads. Thus, although it contains less enzymes In the desizing application of alginate beads with 7% enzyme concentration by weight It was found that better results were obtained.
Ornek 2 - Amilaz çözeltisi Hasil sökme uygulamasi için %7 ve %10 oraninda amilaz enzim içeren sulu çözeltiler hazirlandi. Uygulamadaki performansini test etmek için amilaz enzimi içeren sulu çözelti 60°C,de 30 dk hasil sökme uygulamasina maruz birakildi. Elde edilen sonuçlar Tablo 2'de verilmistir. TEGEWA testi ile enzim performanslari ölçüldü. TEGEWA degeri enzim performansi ile dogru orantili olarak degismektedir. Example 2 - Amylase solution Aqueous solutions containing 7% and 10% amylase enzyme for desizing application was prepared. Aqueous solution containing amylase enzyme to test its performance in application It was exposed to desizing application at 60°C for 30 minutes. The results obtained are in Table 2 has been given. Enzyme performances were measured with the TEGEWA test. TEGEWA value enzyme It varies in direct proportion to its performance.
Amilaz konsantrasyonu (%) TEGEWA Yapilan denemeler sonucunda amilaz çözeltilere kiyasla sistemde amilaz içeren aljinat boncuklar bulundugunda daha yüksek TEGEWA degerleri bulunmustur. Bunda aljinatin iyonik çapraz baglama ile jel olusturmasinin enzime daha etkili bir bariyer olusturmasi etkili olmustur. Amylase concentration (%) TEGEWA As a result of the experiments, alginate containing amylase was more effective in the system compared to amylase solutions. Higher TEGEWA values were found when beads were present. alginatin in this Gel formation by ionic cross-linking creates a more effective barrier to the enzyme. It has been effective.
Ornek 3 - Aljinat ile enkapsüle katalaz Antiperoksit enzim uygulamasi için agirlikça %1,0”lik sodyum aljinat sulu çözeltisine agirlikça %1,5 ve %1,8 oraninda katalaz enzimi eklenerek katalaz içeren aljinat çözeltileri hazirlandi. Bu çözeltiler 0,2 M°lik kalsiyum klorür çözeltilerine damlatilarak kalsiyum aljinat boncuklari elde edildi. Uygulamadaki performansini test etmek için antiperoksit enzimi içeren aljinat çözeltisi ve kalsiyum aljinat boncuk örnekleri antiperoksit enzim uygulamasina maruz birakildi. Bu amaçla 8 gr/lt NaOH (%45°1ik) ve 10 gr/lt H202 yapildiktan sonra banyo 45°C”ye sogutulup pH 5-5,5°ye ayarlandi. Sonraki adimda 45°C5de 20 dk 0,35 gr/lt'lik banyoda bekletildi. Belli süreler sonunda ortamda kalan peroksit miktari ölçülerek enzimin etkinligi belirlendi. Elde edilen sonuçlar Tablo 3”te verilmistir. Example 3 - Catalase encapsulated with alginate For antiperoxide enzyme application, add 1.0% sodium alginate aqueous solution by weight. Alginate solutions containing catalase by adding 1.5% and 1.8% catalase enzyme by weight was prepared. These solutions were dropped into 0.2 M calcium chloride solutions to dissolve calcium. alginate beads were obtained. antiperoxide to test its performance in application samples of alginate solution and calcium alginate beads containing enzyme antiperoxide enzyme was subjected to the practice. For this purpose, 8 g/lt NaOH (45% 1% and 10 g/lt H2O2) After this, the bath was cooled to 45°C and the pH was adjusted to 5-5.5°. In the next step It was kept in a 0.35 g/lt bath for 20 minutes at 45°C. remaining in the environment after certain periods of time The effectiveness of the enzyme was determined by measuring the amount of peroxide. The results obtained are in Table 3 has been given.
Enkapsülasyon konsantrasyonu 5.dk (ml) 15. dk (ml) 20.dk (ml) metodu (%) En iyi sonuç agirlikça %l,8 enzim konsantrasyonu olan aljinat boncuklarinda kaydedilmistir. Örnek 4 - Katalaz çözeltisi Antiperoksit enzim uygulamasi için agirlikça %1,8`lik sulu katalaz çözeltileri hazirlandi. Encapsulation concentration 5th minute (ml) 15th minute (ml) 20th minute (ml) method (%) The best results are obtained with alginate beads with an enzyme concentration of 1.8% by weight. has been recorded. Example 4 - Catalase solution For antiperoxide enzyme application, 1.8% aqueous catalase solutions by weight were prepared.
Uygulamadaki performansini test etmek için sulu katalaz çözeltileri antiperoksit eiiziiii test uygulamasina maruz birakildi. Bu amaçla 8 gr/lt NaOH (%45,lik) ve 10 gr/lt HzOz (%50) içeren banyo hazirlanip, 98°C”de 45 dk pH 11-12”de arasi kasar uygulamasi yapildiktan gr/lt°1ik banyoda bekletildi. Belli süreler sonunda ortamda kalan peroksit miktari ölçülerek katalazin etkinligi belirlendi. Elde edilen sonuçlar Tablo 4”te verilmistir. konsantrasyonu (%) 5. dk (ml) 15. dk (ml) 20. dk (ml) Yapilan denemeler sonucunda sulu katalaz çözeltilerine kiyasla sistemde alijnat boncuk içeren formülasyonlarda uygulama sonrasinda ortamda daha az peroksit bulunmustur. Aqueous catalase solutions were tested for antiperoxide efficacy to test its performance in practice. was subjected to the practice. For this purpose, 8 g/lt NaOH (45%) and 10 g/lt HzOz (50%) After preparing the bath containing the product and applying bleach at 98°C for 45 minutes at pH 11-12. It was kept in a gr/lt°1 bath. By measuring the amount of peroxide remaining in the environment after certain periods of time, The effectiveness of catalase was determined. The results obtained are given in Table 4. concentration (%) 5th minute (ml) 15th minute (ml) 20th minute (ml) As a result of the experiments, there were no alijnate beads in the system compared to aqueous catalase solutions. Less peroxide was found in the environment after application in formulations containing
Bunda aljinatin iyonik çapraz baglama ile jel olusturmasinin enzime daha etkili bir bariyer olusturmasi etkili olmustur. Örnek 5 - Aliinat ile enkapsüle selülaz Antipilling enzim uygulamasi için agirlikça %lllik sodyum aljinat çözeltisine agirlikça Bu çözeltiler 0,2 M`lik kalsiyum klorür çözeltilerine damlatilarak kalsiyum aljinat boncuklari elde edildi. Uygulamadaki performansini test etmek için banyoda 55 OC”de pH 57de 60 dk uygulama yapildiktan sonra 2000 devirde boncuklanma testi yapildi. In this, alginate forming a gel with ionic cross-linking provides a more effective barrier to the enzyme. Its creation has been effective. Example 5 - Cellulase encapsulated with aliinate For antipilling enzyme application, add 1% by weight sodium alginate solution. These solutions were dropped into 0.2 M calcium chloride solutions to form calcium alginate. beads were obtained. To test its performance in application, pH temperature was adjusted in the bath at 55 OC. After 60 minutes of application at 57°C, the pilling test was performed at 2000 rpm.
Boncuklanma degerleri 1-5 arasinda degisen bir skaladir. Antipilling performansi arttikça kumas üzerinde uygulama sonrasi daha az boncuk olusmakta ve boncuklanina degeri artmaktadir. 5 anti-ppling performansi en yüksek, 1 ise anti-pilling performansi en düsük olan için verilmektedir. Elde edilen sonuçlar Tablo 5°te verilmistir. Pilling values are on a scale ranging from 1-5. As antipilling performance increases After application on the fabric, fewer beads are formed and the beading value is reduced. increasing. 5 is the highest anti-pilling performance, 1 is the lowest anti-pilling performance It is given for what is. The results obtained are given in Table 5.
Enkapsülasyon metodu Selülaz konsantrasyonu (0/0) Boncuklanma degeri A1 jinat boncuk 10,0 4 A1 jinat boncuk 13 ,3 Aljinat çözeltisi 10,0 2 Aljinat çözeltisi 13,3 3 En iyi sonuç agirlikça %10 enzim konsantrasyonu olan aljinat boncuklarinda kaydedilmistir. Örnek 6 - Selülaz çözeltisi Anti-pilling enzim uygulamasi için %10 ve 13,3°lük sulu selülaz enzimi çözeltisi hazirlandi. Uygulamadaki performansini test etmek için banyoda 55 °C3de pH Slde 60 dk uygulama yapildiktan sonra 2.000 devirde boncuklanma testi yapildi. Elde edilen sonuç-lar Tablo 6°da verilmistir. Encapsulation method Cellulase concentration (0/0) Pilling value A1 ginat beads 10.0 4 A1 ginat beads 13,3 Alginate solution 10.0 2 Alginate solution 13.3 3 The best results are obtained with alginate beads with 10% enzyme concentration by weight. has been recorded. Example 6 - Cellulase solution 10% and 13.3° aqueous cellulase enzyme solution for anti-pilling enzyme application was prepared. To test its performance in application, it was heated in a bath at 55 °C and pH for 60 minutes. After application, pilling test was performed at 2,000 cycles. Obtained results It is given in Table 6.
Selülaz konsantrasyonu (%) Boncuklanma degeri ,0 1 13,3 2 Yapilan denemeler sonucunda sulu selülaz çözeltilerine kiyasla sistemde alijnat boncuk içeren formülasyonlarda uygulama sonrasi daha az boncuk olusarak antipilling perfomansi ile dogru orantili olarak daha yüksek boncuklanma degeri bulunmustur. Bunda aljinatin iyonik çapraz baglama ile jel olusturmasmm enzime daha etkili bir bariyer olusturmasi etkili olmustur. Cellulase concentration (%) Pilling value ,0 1 13.3 2 As a result of the experiments, there were no alijnate beads in the system compared to aqueous cellulase solutions. antipilling performance by forming fewer beads after application in formulations containing A higher pilling value was found in direct proportion to the . alginatin in this Gel formation by ionic cross-linking creates a more effective barrier to the enzyme. It has been effective.
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| PCT/TR2020/051109 WO2021133302A1 (en) | 2019-12-26 | 2020-11-16 | Encapsulated enzymes and the usage thereof in textile applications |
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